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908 Devices Plans to Target Proteomics Market With Capillary Electrophoresis Separation Tech


NEW YORK — With new hires and the appointment of several new members to its scientific advisory board, portable mass spectrometry firm 908 Devices is moving to target the proteomics market.

This month, the company announced the formation of a dedicated proteomics panel within its SAB, composed of six leading proteomics researchers spanning a range of research areas. It also hired Will Thompson as principal scientist, formerly an assistant research professor of proteomics and metabolomics at Duke University and associate director of the Duke Proteomics Core.

Within the life sciences, Boston-based 908 has traditionally focused on the biopharma market, positioning its ZipChip capillary electrophoresis-based sample separation platform and Rebel benchtop mass spec system for use in biologics characterization and bioprocessing.

Chris Brown, 908's chief technology officer, said, however, that the company has consistently received inquiries from current and potential customers about its tools' proteomics applications.

That, combined with increasing interest in proteomics by researchers and investors more generally, convinced the company to explore moving into the space, he said.

The six members of the SAB's proteomics panel are Ileana Cristea, professor of molecular biology at Princeton University; Jennifer Van Eyk, professor of medicine at Cedars-Sinai Medical Center; Anne-Claude Gingras, senior investigator at the Lunenfeld-Tanenbaum Research Institute; Jesper Olsen, professor and vice director of the Novo Nordisk Foundation Center for Protein Research at the University of Copenhagen; Renã Robinson, associate professor of chemistry at Vanderbilt University; and John Yates, professor of molecular medicine at Scripps Research Institute.

Additionally, with the hire of Thompson and others, 908 is building "expertise in house around this domain," Brown said. The company has also established relationships and collaborations with proteomics researchers outside the SAB panel, he said, adding that it plans to present some of this work at this fall's American Society for Mass Spectrometry annual meeting.

The ZipChip device is the centerpiece of 908's proteomics strategy. Capillary electrophoresis, or CE, has long been considered a potential separations tool for proteomics research, but thus far it has been much more widely used for biopharma work and DNA analysis, while liquid chromatography has predominated in proteomics research.

CE separates proteins and peptides based on their masses and charges. The approach has potential advantages compared to LC, perhaps most notably speed. Brown said that the ZipChip can achieve a separation in around eight minutes that would take LC around two hours.

"You can get extremely sharp peaks, much sharper than what you can typically get with LC," Olsen said. "That gives you the advantage of [being able] to concentrate a lot of signal in a very short period of time, which gives you a much stronger [signal] in the mass spectrometer compared to an equivalent sample analyzed by LC."

One of the main factors limiting the use of CE in proteomics has been the relatively small sample volumes the technology is able to work with, said Olsen.

"That has been the main issue," he said. "The capacity was simply too low, so you couldn't load a sufficient amount of peptides to really run complex mixtures."

The shift within proteomics toward smaller samples, including single-cell proteomics, as well as the development of faster and more sensitive mass specs capable of analyzing such small samples, has made CE a potentially useful tool.

"Mass specs now have such fast scanning rates that they can analyze up to 40 or even 100 peptides per second," he said. "So they have the sequencing speed needed to cope with this very sharp chromatography."

Regarding the ZipChip specifically, he said that its chip-based format made it a potentially attractive device for proteomics researchers.

"Everything is integrated," he said. "They have a source that you can click directly onto the mass spectrometer, and from what I have seen, it can be adapted to most of the popular mass spec instruments. So that makes it easy and accessible for the wider community."

Olsen said that his lab was interested in exploring the utility of CE for experiments using small sample volumes like single-cell proteomics and clinical work.

Brown said that while the proteomics field's move toward smaller sample volumes provided an opportunity for the ZipChip, 908 was also interested in modifying the technology to make it more compatible with larger sample volumes.

He said that could involve work on the sample preparation side of things, including potentially incorporating some form of sample concentration into the system or possibly partnering with another firm to incorporate their sample prep technology. He cited the example of proteomics startup Seer, which uses nanoparticles to fractionate and enrich proteomics samples prior to mass spec analysis.

"We're working both sides of it," he said. "Can we accommodate larger sample sizes and condense them down to smaller volumes for use with CE, and at the same time, are there large pockets of proteomics that are intrinsically oriented towards smaller sample sizes where we just have a direct advantage?"

Another area where 908 will look to make inroads is in top-down proteomics. CE is already somewhat more common in this area than in bottom-up proteomics, with researchers including Scripps' Yates having explored its utility for top-down research.

This month, the Consortium for Top-Down Proteomics launched a new initiative to develop guidelines for the use of CE in top-down research. In a statement, the organization noted that "the high resolution provided by CE will be particularly valuable in separating various proteoforms and non-covalent protein complexes present in biological and biopharmaceutical samples."

Neil Kelleher, director of the Chemistry of Life Processes Institute at Northwestern University and a leading top-down proteomics researcher, said that CE is complementary to reversed-phase LC in top-down research, allowing separation and identification of proteoforms not detectable using LC. In his opinion, it is the best separation option for native-mode protein mass spec, which analyzes proteins in their folded state.

"In denatured, top-down discovery mode, you can identify new proteoforms if you use both [LC and CE]," he said, noting in particular that CE is more effective for separating phospho-proteoforms. "In native mode, there really is no analogy in the LC world [to CE]," he added.

Kelleher, who is not part of 908's proteomics panel, said he had communicated with the company about its CE technology.

908 is not alone in the CE space. Sciex, which has been one of the major providers of CE systems for top-down proteomics research, in January acquired Fremont, California-based CE firm Intabio, though that deal was focused primarily on the biopharma space rather than the proteomics market.

Also, in June, Thermo Fisher Scientific signed an agreement with Ontario, Canada-based Advanced Electrophoresis Solutions, under which the firms will jointly promote Thermo Fisher's mass spectrometry systems for biopharma and proteomics applications and AES' whole-column imaging detection capillary electrophoresis systems for protein separation, quantification, and characterization.

While the ZipChip is the focus of 908's proteomics push, Brown said the company was also exploring possible applications of its Rebel desktop mass spec system in the proteomics space, most likely for targeted analyses.

"You can imagine a future where maybe, if you are doing a directed proteomics assay — not a wide-scale discovery experiment — [and] if you know what you are looking for, [the Rebel] may be able to do the job and sort of democratize access to those sorts of assays," he said. "We're not going to put Thermo or Bruker out of business."